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EC Tree
The taxonomic range for the selected organisms is: Escherichia coli The enzyme appears in selected viruses and cellular organisms
Synonyms
neuron-specific enolase, enolase, neuron specific enolase, alpha-enolase, gamma-enolase, enolase 1, beta-enolase, yeast enolase, enolase 2, eno-1,
more
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2-phospho-D-glycerate hydro-lyase
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2-phosphoglycerate dehydratase
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2-phosphoglycerate enolase
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2-phosphoglyceric dehydratase
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alpha,alpha-enolase
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beta,beta-enolase
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gamma,gamma-enolase
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hydratase, phosphoenolpyruvate
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Laminin binding protein
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Major allergen Alt a 11
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neuron-specific enolase
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Non-neural enolase
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phosphoenolpyruvate hydratase
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Phosphopyruvate hydratase
Skeletal muscle enolase
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enolase
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Phosphopyruvate hydratase
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Phosphopyruvate hydratase
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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2-phospho-D-glycerate hydro-lyase (phosphoenolpyruvate-forming)
Also acts on 3-phospho-D-erythronate.
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
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r
2-phospho-D-glycerate
phosphoenolpyruvate
2-phospho-D-glycerate
phosphoenolpyruvate
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?
2-phospho-D-glycerate
phosphoenolpyruvate
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2-phospho-D-glycerate
phosphoenolpyruvate
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2-phospho-D-glycerate
phosphoenolpyruvate
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r
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
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r
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additional information
interaction with RNase E of the RNA degradasome, enolase recognition site for RNase E conserved in gamma-proteobacteria
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additional information
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interaction with RNase E of the RNA degradasome, enolase recognition site for RNase E conserved in gamma-proteobacteria
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Mg2+
coordinated in catalytic site of enolase
Mg2+
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activation
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additional information
additional information
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260
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pH 8.1, room temperature
additional information
additional and independent function beyond glycolytic enzyme function, association of enolase to the RNA degrasome, role in RNA metabolism predicted
additional information
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additional and independent function beyond glycolytic enzyme function, association of enolase to the RNA degrasome, role in RNA metabolism predicted
additional information
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additional information
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SwissProt
brenda
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as part of the degradosome complex
brenda
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45545
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2 * 45545, mass spectrometry and X-ray crystallography
46000
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2 * 46000, SDS-PAGE
90000
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sedimentation velocity and sedimentation equilibrium experiments
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dimer
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2 * 46000, SDS-PAGE
dimer
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2 * 45545, mass spectrometry and X-ray crystallography
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1.6 A resolution, co-crystallization of enolase with a synthetic peptide corresponding to residues 833 to 850 from RNase E determined, asymmetric binding of a single molecule of RNase E to a conserved cleft at the interface of the enolase dimer
using the sitting drop method, co-crystallized with Mg2+
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using gel filtration chromatography
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Spring, T.G.; Wold, F.
The purification and characterization of Escherichia coli enolase
J. Biol. Chem.
246
6797-6802
1971
Escherichia coli
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Spring, T.G.; Wold, F.
Enolase from Escherichia coli
Methods Enzymol.
42C
323-329
1975
Escherichia coli
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Dannelly, H.K.; Reeves, H.C.
Purification and characterization of enolase from Escherichia coli
Curr. Microbiol.
17
265-268
1988
Escherichia coli
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Kuhnel, K.; Luisi, B.F.
Crystal structure of the Escherichia coli RNA degradosome component enolase
J. Mol. Biol.
313
583-592
2001
Escherichia coli
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Chandran, V.; Luisi, B.F.
Recognition of enolase in the Escherichia coli RNA degradosome
J. Mol. Biol.
358
8-15
2006
Escherichia coli (P0A6P9), Escherichia coli
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